Ribosomal binding and antibacterial activity of ethylene glycol ‐bridged apidaecin Api137 and oncocin Onc112 conjugates

In conclusion, Api137/Onc112‐conjugates showed increased antimicrobial activities against P. aeruginosa and PrAMP‐susceptible and ‐resistant E. coli most likely because of improved membrane interactions, whereas the interaction to the 70S ribosome was most likely not improved relying still on the independent apidaecin‐ and oncocin‐type binding modes. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd. Proline‐rich antimicrobial peptides intracellularly inhibit 70S ribosomes utilizing an apidaecin‐ or oncocin‐type binding. Development of a bifunctional inhibitor targeted for bridging both binding sites in order to improve inhibition of protein translation and antimicrobial activity. Fluorescence polarization‐based interaction studies proved described binding modes.
Source: Journal of Peptide Science - Category: Biochemistry Authors: Tags: Research Article Source Type: research